Abstract
The fragmentation of free tenfold protonated ubiquitin in intense 70femtosecond pulses of 90eV photons from the FLASH facility was investigated. Mass spectrometric investigation of the fragment cations produced after removal of many electrons revealed fragmentation predominantly into immonium ions and related ions, with yields increasing linearly with intensity. Ionization clearly triggers a localized molecular response that occurs before the excitation energy equilibrates. Consistent with this interpretation, the effect is almost unaffected by the charge state, as fragmentation of sixfold deprotonated ubiquitin leads to a very similar fragmentation pattern. Ubiquitin responds to EUV multiphoton ionization as an ensemble of small peptides.
Original language | English |
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Pages (from-to) | 10741-10745 |
Number of pages | 5 |
Journal | Angewandte Chemie - International Edition |
Volume | 55 |
Issue number | 36 |
DOIs | |
Publication status | Published - 26-Aug-2016 |
Keywords
- free-electron lasers
- mass spectrometry
- multiphoton ionization
- photoionization
- proteins
- SOFT-X-RAY
- SPECTROSCOPY
- PROTEINS
- PEPTIDES
- ENERGY
- VUV